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Modulating Hydrogen Bonded Self–assembled Patterns and Morphological Features by a Change in Side Chain of Third Amino Acid of Synthetic γ‐ Amino Acid Based Tripeptides
Author(s) -
Konda Maruthi,
Bhowmik Soumitra,
Mobin Shaikh M.,
Biswas Sagar,
Das Apurba K.
Publication year - 2016
Publication title -
chemistryselect
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.437
H-Index - 34
ISSN - 2365-6549
DOI - 10.1002/slct.201600557
Subject(s) - tripeptide , amino acid , side chain , chemistry , peptide , stereochemistry , oligopeptide , self assembly , hydrogen bond , crystallography , molecule , biochemistry , organic chemistry , polymer
Self‐assembled structure and functions of peptides could be achieved by the design and synthesis of hybrid peptides. Here, we report structural and morphological studies of designed hybrid tripeptides Boc‐Gpn‐Aib‐Xaa‐OMe (where Xaa=Leu(L) for 1 and Phe(F) for 2 ), which show different conformations both in solid and solution states. The conformational modulations are achieved by the design and synthesis of reported peptides 1 and 2 by suitable choice of conventional and non‐conventional amino acid building blocks and slight change in side‐chain of third amino acids of tripeptides. The conformational modulations exhibited by peptides 1 and 2 are well probed and confirmed using Single crystal XRD, FT‐IR, CD and 2D NMR studies. The morphological studies of peptides 1 and 2 show different self‐assembled morphological preferences in THF – water (1:1) under similar experimental conditions.